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Allosteric signaling in biological molecules, which may be viewed as specificaction at a distance due to localized perturbation upon binding of ligands orchanges in environmental cues, is pervasive in biology. Phenomenological MWCand KNF models galvanized research for over five decades, and these modelscontinue to be the basis for describing the allostery in an array of systems.However, understanding allosteric signaling and the associated dynamics betweendistinct allosteric states is challenging. In this review, we first describesymmetry and rigidity as essential requirements for allosteric proteins. Thegeneral features, with MWC and KNF as two extreme scenarios, emerge whenallosteric signaling is viewed from an energy landscape perspective. To gobeyond the general theories, we describe computational tools to predict thenetwork of residues that carry allosteric signals. Methods to obtain molecularinsights into the dynamics of allosteric transitions are briefly mentioned. Theutility of the methods is illustrated by applications to systems ranging frommonomeric proteins to multisubunit proteins. Finally, the role allostery playsin the functions of ATP-consuming molecular machines, bacterial chaperoninGroEL and molecular motors, is described. Although universal molecularprinciples governing allosteric signaling do not exist, we can draw thefollowing general conclusions. (1) Multiple pathways connecting allostericstates are highly heterogeneous. (2) Allosteric signaling is exquisitelysensitive to the architecture of the system, which implies that the capacityfor allostery is encoded in the structure itself. (3) The mechanical modes thatconnect distinct allosteric states are robust to sequence variations. (4)Extensive investigations of allostery in Hemoglobin and more recently GroEL,show that a network of salt-bridge rearrangements serves as allostericswitches.

Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines